Special Issue "Lipid Metabolism"

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A special issue of Biology (ISSN 2079-7737).

Deadline for manuscript submissions: closed (30 September 2014)

Special Issue Editor

Guest Editor
Prof. Dr. Annette Graham
Life Sciences, School of Health and Life Sciences, and the Institute for Applied Health Research, Glasgow Caledonian University, Glasgow, UK
Website: http://www.gcu.ac.uk/hls/staff/professorannettegraham/
E-Mail: Ann.Graham@gcu.ac.uk
Interests: Intracellular lipid transport in health and disease; lipid and lipoprotein metabolism; vascular contributions to diabetes and Alzheimer’s disease

Special Issue Information

Dear Colleagues,

It is becoming increasingly evident that intracellular proteins can specifically regulate the direction of lipid transport within cells, thereby influencing the storage, synthesis and export of lipids, and the activity of nuclear receptor transcription factors involved in lipid and lipoprotein metabolism. Defective intracellular lipid transport may also contribute to a number of disease states, including metabolic disorders and tumorigenesis.
For this special issue, we invite research articles on aspects of lipid transport within cells and tissues, and particularly those which contribute to our understanding of the role of intracellular lipid transporters in pathological conditions.

Prof. Annette Graham
Guest Editor

Submission

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are refereed through a peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biology is an international peer-reviewed Open Access quarterly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 300 CHF (Swiss Francs). English correction and/or formatting fees of 250 CHF (Swiss Francs) will be charged in certain cases for those articles accepted for publication that require extensive additional formatting and/or English corrections.

Published Papers (5 papers)

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Displaying article 1-5
p. 892-921
by , , , ,  and
Biology 2014, 3(4), 892-921; doi:10.3390/biology3040892
Received: 7 November 2014; in revised form: 4 December 2014 / Accepted: 8 December 2014 / Published: 15 December 2014
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(This article belongs to the Special Issue Lipid Metabolism)
p. 866-891
by , , , , ,  and
Biology 2014, 3(4), 866-891; doi:10.3390/biology3040866
Received: 2 October 2014; in revised form: 22 November 2014 / Accepted: 26 November 2014 / Published: 4 December 2014
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(This article belongs to the Special Issue Lipid Metabolism)
abstract graphic
p. 801-830
by , , , , ,  and
Biology 2014, 3(4), 801-830; doi:10.3390/biology3040801
Received: 12 September 2014; in revised form: 2 November 2014 / Accepted: 5 November 2014 / Published: 19 November 2014
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(This article belongs to the Special Issue Lipid Metabolism)
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p. 781-800
by , , , , Jr., ,  and
Biology 2014, 3(4), 781-800; doi:10.3390/biology3040781
Received: 2 October 2014; in revised form: 23 October 2014 / Accepted: 28 October 2014 / Published: 14 November 2014
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(This article belongs to the Special Issue Lipid Metabolism)
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p. 536-550
by , , , , , , , ,  and
Biology 2014, 3(3), 536-550; doi:10.3390/biology3030536
Received: 23 June 2014; in revised form: 29 July 2014 / Accepted: 5 August 2014 / Published: 25 August 2014
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Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Type of Paper: Article
Title: Cellular Localization and Trafficking of the Human ABCG1 Transporter
Authors: Edward B. Neufeld 1,5, Katherine O’Brien 1, Avram D. Walts 1, John A. Stonik 2, Steven J. Demosky, Jr 2, Steven Sabol 2, Daniela Malide 3, Christian A. Combs 3 and Alan T. Remaley 2
Affiliations: 1. Lipid Trafficking Core, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD USA; E-Mail: neufelde@nhlbi.nih.gov
2. Lipoprotein Metabolism Section, Vascular Medicine Branch, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD USA; E-Mail: aremaley1@cc.nih.gov
3. NHLBI Light Microscopy Core Facility, National Institutes of Health, Bethesda, MD USA
4. Lipoprotein and Atherosclerosis Research, Cardiovascular Research Institute, MedStar Research Institute, Washington Hospital Center
Abstract: We have developed a suitable heterologous cell expression system to study the localization, trafficking, and site(s) of function of the human ABCG1 transporter. Stable expression of GFP-tagged human ABCG1 in a HeLa cell line that lacks endogenous ABCG1, ABCG4 and ABCA1 enhanced cholesterol efflux to liposomes and lipoproteins, but not to apoA-I. ABCG1-GFP expression increased the cholesterol content on the cell surface and endosomes, and this excess cholesterol was removed by HDL. ABCG1-GFP trafficked from its site of synthesis in the ER to the cell surface and then to late endocytic vesicles. BFA and U18666A reduced ABCG1-GFP expression on the cell surface and endosomes as well as ABCG1-mediated cellular cholesterol efflux to HDL, consistent with a role for plasma membrane and endosomal ABCG1 in cholesterol efflux. Monensin blocked delivery of ABCG1-GFP to the cell surface and trapped PM-derived ABCG1-GFP in late endocytic vesicles but did not alter ABCG1-mediated cellular cholesterol efflux, suggesting a role for late endosomal ABCG1 in cholesterol efflux. Hydrolysis of cellular SM markedly enhanced cycling of ABCG1 between endosomes and the cell surface and increased ABCG1-mediated cellular cholesterol efflux to HDL, consistent with a role for ABCG1 (but not SM) cycling between late endosomes and the cell surface in cellular cholesterol efflux. Taken together, these studies establish that ABCG1 at the cell surface and endosomes can generate mobile pools of cholesterol that are available to transfer to extracellular acceptors with a lipid surface.

Type of Paper: Article
Title: The Human ABCG1 Transporter Mobilizes Plasma Membrane and Endosomal Non-Sphingomyelin-Associated Cholesterol for Efflux and Esterification
Authors: Edward B. Neufeld 1,5, Katherine O’Brien 1, Avram D. Walts 1, John A. Stonik 2, Daniela Malide 3, Christian A. Combs 3 and Alan T. Remaley 2
Affiliations: 1. Lipid Trafficking Core, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD USA; E-Mail: neufelde@nhlbi.nih.gov
2. Lipoprotein Metabolism Section, Vascular Medicine Branch, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD USA; E-Mail: aremaley1@cc.nih.gov
3. NHLBI Light Microscopy Core Facility, National Institutes of Health, Bethesda, MD USA
Abstract: We have previously shown that GFP-tagged human ABCG1 on the cell surface and in late endosomes enhances cellular cholesterol efflux to extracellular acceptors with a lipid surface (e.g., HDL, liposomes). In the present study, we examined ABCG1-induced changes in membrane cholesterol distribution, organization, and mobility. ABCG1-GFP expression increased the amount of mobile, non-sphingomyelin(SM)-associated cholesterol at the plasma membrane and endosomes, but did not alter the amount of SM-associated-cholesterol or SM. Non-SM-associated-cholesterol mobilized by ABCG1 rapidly cycled between the cell surface and endosomes and was available for removal from the cell surface by extracellular acceptors, or, relocated to intracellular sites of esterification. ABCG1-GFP expression increased resistance to both amphotericin B- and lysenin-induced cytolysis, and generated a pool of detergent-resistant, non-SM-associated plasma membrane cholesterol, consistent with altered organization of both plasma membrane cholesterol and SM. ABCG1 itself was found to reside in detergent-soluble membrane domains. We propose that plasma membrane and endosomal ABCG1 residing at the phase boundary between ordered (Lo) and disordered (Ld) membrane lipid domains alters SM and cholesterol organization thereby increasing cholesterol flux between Lo and Ld and hence, the amount of cholesterol available for removal by either extracellular (efflux) or intracellular cholesterol acceptors (esterification).

Type of Paper: Article
Title: Genetic risk scores associated with baseline lipoprotein subfraction concentrations do not associate with their responses to fenofibrate
Authors: Alexis C. Frazier-Wood 1,*, Mary K. Wojczynski 2, Ingrid B. Borecki 2, Paul N. Hopkins 3, Chao-Qiang Lai 4, Jose M. Ordovas 4,5,6, Robert J. Straka 7, Micheal Y. Tsai 8, Hemant K. Tiwari 9 and Donna K. Arnett 10
Affiliations: 1. USDA / ARS Children’s Nutrition Research Center, Baylor College of Medicine, Houston, Texas USA; E-Mail: LekkiWood@Gmail.com
2. Department of Genetics, Washington University School of Medicine, St. Louis, MO, USA
3. Department of Internal Medicine, University of Utah, Salt Lake City, UT, USA
4. Nutrition and Genomics Laboratory, Jean Mayer-US Department of Agriculture Human Nutrition Research Center on Aging, Tufts University, Boston, MA, USA
5. The Department of Epidemiology and Population Genetics. Centro Nacional Investigación Cardiovasculares (CNIC) Madrid, Spain.
6. IMDEA Food, Madrid, Spain.
7. Department of Experimental and Clinical Pharmacology, College of Pharmacy, University of Minnesota, Minneapolis, MN 55455
8. Department of Laboratory Medicine and Pathology, University of Minnesota, MN
9. Section on Statistical Genetics, University of Alabama at Birmingham, School of Public Health, AL, United States
10. Department of Epidemiology, University of Alabama at Birmingham, School of Public Health, AL, United States
Abstract: Lipoprotein subclass concentrations are modifiable markers of cardiovascular disease risk. Fenofibrate is known to show beneficial effects on lipoprotein subclasses, but little is known about the role of genetics in mediating the responses of lipoprotein subclasses to fenofibrate. A recent genomewide association study (GWAS) associated several single nucleotide polymorphisms (SNPs) with lipoprotein measures, and validated these associations in two independent populations. We used this information to constructed genetic risk scores (GRSs) for fasting lipoprotein measures at baseline (pre-fenofibrate), and aimed to examine whether these GRSs also associated with the responses of lipoproteins to fenofibrate.. Fourteen lipoprotein subclass measures were assayed in 817 men and women before and after a three week fenofibrate trial. We set significance at a Bonferroni corrected alpha<.05 (P<.004). Twelve subclass measures changed with fenofibrate administration (each P=.003-<.0001). Mixed linear models which controlled for age, sex, body mass index (BMI), smoking status, pedigree and study-center, revealed that GRSs were associated with eight baseline lipoprotein measures (P<.004), however no GRS was associated with fenofibrate response. These results suggest that the mechanisms for changes in lipoprotein subclass concentrations with fenofibrate treatment are not mediated by the genetic risk for fasting levels.

Last update: 24 June 2014

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